Emmanuel Ampofo

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Protein kinase CK2, a ubiquitous serine/threonine kinase in control of a variety of crucial cellular functions, is composed of catalytic α- and α′-subunits and non-catalytic β-subunits which form holoenzymes such as CK2(αβ)2, CK2αα′β2, or CK2(α′β)2. In addition, there is ample evidence for the occurrence of the individual subunits beside the holoenzyme.(More)
The von Hippel-Lindau tumour suppressor gene encodes a protein with 213 amino acids, which is known to be part of an E3-ubiquitin ligase targeting the HIF-1alpha transcription factor as well as to form a complex with p53. The VHL protein can be phosphorylated by protein kinase CK2 at serines 33, 38 and 43. However, the role of VHL phosphorylation in the(More)
Protein kinase CK2 is a pleiotropic enzyme, which is implicated in the regulation of numerous biological processes. It seems to regulate the various functions by binding to other proteins and by phosphorylation of many different substrates. Here, we identified the activating transcription factor 4 (ATF4), an essential component of the ER stress signaling,(More)
Protein kinase CK2 is an ubiquitously expressed serine/threonine kinase. The protein levels along with CK2 activity are highly elevated in tumour cells where it protects cells from apoptosis. Accordingly, inhibition of CK2 is known to induce programmed cell death, making it a promising target for cancer therapy. Analysis of the different behaviour of(More)
INTRODUCTION Thrombus formation is a complex process, which is characterized by the dynamic interaction of platelets, leukocytes and endothelial cells. The activation of these cells is strictly mediated by different phospho-regulated signaling pathways. Recently, it has been reported that inhibition of protein kinase CK2 affects platelet function by(More)
Inflammatory endothelial processes are regulated by the nuclear factor-κB (NF-κB) pathway, which involves phosphorylation of p65. Because p65 is a substrate of CK2, we herein investigated, whether this pleiotropic protein kinase may be a beneficial anti-inflammatory target. For this purpose, we analyzed in human dermal microvascular endothelial cells(More)
BACKGROUND Ischemia and reperfusion (I/R) causes tissue injury by inflammatory processes. This involves the upregulation of endothelial surface proteins by phospho-regulated signaling pathways, resulting in enhanced interactions of leukocytes with endothelial cells. Recently, we found that protein kinase CK2 is a crucial regulator of leukocyte-mediated(More)
BACKGROUND Protein kinase CK2 is a pleiotropic enzyme which is ubiquitously expressed in eukaryotic cells. Several years ago CK2 was found to be associated with the mammalian endoplasmic reticulum. So far nothing is known about the function of CK2 at the ER. METHODS CK2 phosphorylation sites in the polypeptide chain of Sec63 were mapped using deletion(More)
BACKGROUND Ischemia-reperfusion (I/R) induces tissue inflammation, which is characterized by an increased leukocyte-endothelial cell interaction and leukocyte transmigration. These processes are mediated by the activation of the nuclear factor (NF)κB signaling pathway, resulting in an elevated expression of specific adhesion molecules. The phytochemical(More)
The proteoglycan nerve/glial antigen (NG) 2 is expressed on multiple cell types and mediates cell proliferation and migration. However, little is known about its function in gene regulation. In this study, we demonstrate that in pericytes and glioblastoma cells intercellular adhesion molecule (ICAM)-1, an essential protein for leukocyte adhesion and(More)